偶氮氯膦mA-铌与牛血清白蛋白结合反应及其应用

Study on interaction between chlorophosphonazo-mA-niobium(Ⅴ) and bovine serum albumin and its application

用分光光度法研究了偶氮氯膦-mA-铌配合物与牛血清白蛋白（BSA）结合反应体系。在pH3．0的磷酸氢二钠-柠檬酸缓冲溶液（Mcllvaine）中，随着BSA量的增加，偶氮氯膦mA-铌配合物在542nm波长处吸收峰也随着减小。据此建立了以偶氮氯膦mA-铌配合物为光谱探针，光度法测定蛋白质的新方法。牛血清白蛋白量在0-60mg／L范围内与体系的褪色程度呈良好的线性关系，其相关系数为r=0．9996，摩尔吸光系数为ε542=3．3×10^5L·mol^-1·cm^-1。方法应用于人血清蛋白的测定。

The interaction between CPA-mA -Nb（ V ） and bovine serum albumin （BSA） was investigated. In a pH = 3.0 （Mcllvaine） buffer solution, with the increase of BSA concentration, the absorption peak at 542 nm decreased strikingly. The molar absorptivity is 3.35 × 10^5 L·mol^-1·cm^-1 . Beer＇s law was obeyed in a range from 0 to 60 mg/L. A spectrophotometric method for the determination of protein was established by using CPA-mA -Nb（ Ⅴ ） complex. The proposed method was applied to determination of albumin in human serum albumin and the results were in agreement with certified values. Recoveries of the standard addition for BSA were 98% - 103% with RSD≤2.4% （n = 6）.